Download MendeleyStructure and properties of an engineered transketolase from maize
Gerhardt, S., Echt, S., Busch, M., Freigang, J., Auerbach, G., Bader, G., Martin, W.F., Bacher, A., Huber, R., Fischer, M.(2003) Plant Physiol 132: 1941-1949
- PubMed: 12913150
- DOI: https://doi.org/10.1104/pp.103.020982
- Primary Citation of Related Structures:
1ITZ - PubMed Abstract:
The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of Escherichia coli and mature TK of maize was expressed at a high level in E. coli and cleaved with thrombin, affording plastid TK. The protein in complex with thiamine pyrophoshate was crystallized, and its structure was solved by molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into three domains. The two topologically equivalent active sites are located in the subunit interface region and resemble those of the yeast enzyme.
Organizational Affiliation:
Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany.
